3OSS
The crystal structure of enterotoxigenic Escherichia coli GspC-GspD complex from the type II secretion system
Summary for 3OSS
| Entry DOI | 10.2210/pdb3oss/pdb |
| Descriptor | TYPE 2 SECRETION SYSTEM, GSPC, TYPE 2 SECRETION SYSTEM, SECRETIN GSPD, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | general secretory pathway, hr domain, secretin, lanthanide-binding tag, protein transport |
| Biological source | Escherichia coli More |
| Cellular location | Cell outer membrane : E3PJ86 |
| Total number of polymer chains | 2 |
| Total formula weight | 27387.62 |
| Authors | Korotkov, K.V.,Pruneda, J.,Hol, W.G.J. (deposition date: 2010-09-09, release date: 2011-08-03, Last modification date: 2023-09-06) |
| Primary citation | Korotkov, K.V.,Johnson, T.L.,Jobling, M.G.,Pruneda, J.,Pardon, E.,Heroux, A.,Turley, S.,Steyaert, J.,Holmes, R.K.,Sandkvist, M.,Hol, W.G. Structural and functional studies on the interaction of GspC and GspD in the type II secretion system. Plos Pathog., 7:e1002228-e1002228, 2011 Cited by PubMed Abstract: Type II secretion systems (T2SSs) are critical for secretion of many proteins from Gram-negative bacteria. In the T2SS, the outer membrane secretin GspD forms a multimeric pore for translocation of secreted proteins. GspD and the inner membrane protein GspC interact with each other via periplasmic domains. Three different crystal structures of the homology region domain of GspC (GspC(HR)) in complex with either two or three domains of the N-terminal region of GspD from enterotoxigenic Escherichia coli show that GspC(HR) adopts an all-β topology. N-terminal β-strands of GspC and the N0 domain of GspD are major components of the interface between these inner and outer membrane proteins from the T2SS. The biological relevance of the observed GspC-GspD interface is shown by analysis of variant proteins in two-hybrid studies and by the effect of mutations in homologous genes on extracellular secretion and subcellular distribution of GspC in Vibrio cholerae. Substitutions of interface residues of GspD have a dramatic effect on the focal distribution of GspC in V. cholerae. These studies indicate that the GspC(HR)-GspD(N0) interactions observed in the crystal structure are essential for T2SS function. Possible implications of our structures for the stoichiometry of the T2SS and exoprotein secretion are discussed. PubMed: 21931548DOI: 10.1371/journal.ppat.1002228 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.63 Å) |
Structure validation
Download full validation report
